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P56716 (RP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Oxygen-regulated protein 1
Alternative name(s):
Retinitis pigmentosa RP1 protein homolog
Gene names
Name:Rp1
Synonyms:Orp1, Rp1h
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2095 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Microtubule-associated protein regulating the stability and length of the microtubule-based axoneme of photoreceptors. Required for the differentiation of photoreceptor cells, it plays a role in the organization of the outer segment of rod and cone photoreceptors ensuring the correct orientation and higher-order stacking of outer segment disks along the photoreceptor axoneme. Ref.6 Ref.7

Subunit structure

Interacts (via the doublecortin domains) with microtubules. Interacts with RP1L1. Interacts with MAK. Ref.7 Ref.9 Ref.10

Subcellular location

Cytoplasmcytoskeletoncilium axoneme. Cell projectionciliumphotoreceptor outer segment. Note: Specifically localized in the connecting cilia of rod and cone photoreceptors. Ref.5 Ref.6 Ref.7

Tissue specificity

Expressed in the cell bodies and inner segments of photoreceptors. Not found in liver, spleen, kidney, brain, thymus, muscle, heart, lung and testis.

Induction

Gene expression is stimulated by retinal hypoxia and suppressed by relative retinal hyperoxia.

Domain

The doublecortin domains, which mediate interaction with microtubules, are required for regulation of microtubule polymerization and function in photoreceptor differentiation By similarity.

Disruption phenotype

As early as postnatal day 7, mice have already undergone significant molecular retinal changes. The molecular responses change dramatically during development and were distinct from responses to the disruption of the photoreceptor transcription factors Crx, Pde6b and Nrl. The JNK signaling cascades are specifically compromised in Rp1 defective retinas. Double heterozygotes of Rp1 and Rp1l1 exhibit abnormal outer segment morphology and reduced single rod photosensitivity and dark currents. Ref.8 Ref.9

Sequence similarities

Contains 2 doublecortin domains.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
Sensory transduction
Vision
   Cellular componentCell projection
Cilium
Cytoplasm
Cytoskeleton
   DomainRepeat
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxoneme assembly

Inferred from direct assay Ref.7. Source: UniProtKB

cellular response to light stimulus

Inferred from mutant phenotype PubMed 21052544. Source: MGI

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

microtubule polymerization

Traceable author statement PubMed 23281133. Source: BHF-UCL

negative regulation of microtubule depolymerization

Traceable author statement PubMed 23281133. Source: BHF-UCL

photoreceptor cell development

Inferred from mutant phenotype Ref.8. Source: UniProtKB

photoreceptor cell maintenance

Inferred from mutant phenotype Ref.8. Source: UniProtKB

photoreceptor cell outer segment organization

Inferred from direct assay Ref.6. Source: UniProtKB

retina development in camera-type eye

Inferred from mutant phenotype PubMed 21052544. Source: MGI

retina morphogenesis in camera-type eye

Inferred from mutant phenotype PubMed 21052544. Source: MGI

retinal cone cell development

Inferred from direct assay Ref.6. Source: UniProtKB

retinal rod cell development

Inferred from direct assay Ref.6. Source: UniProtKB

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentaxoneme

Inferred from direct assay Ref.6. Source: UniProtKB

cilium

Inferred from direct assay Ref.5PubMed 12651948. Source: MGI

microtubule associated complex

Inferred from direct assay Ref.7. Source: UniProtKB

photoreceptor connecting cilium

Inferred from direct assay Ref.6. Source: UniProtKB

photoreceptor inner segment

Inferred from direct assay Ref.5. Source: UniProtKB

photoreceptor outer segment

Inferred from direct assay Ref.6Ref.7. Source: UniProtKB

   Molecular_functionmicrotubule binding

Inferred from direct assay Ref.7. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20952095Oxygen-regulated protein 1
PRO_0000097411

Regions

Domain35 – 11783Doublecortin 1
Domain157 – 23680Doublecortin 2
Compositional bias655 – 6606Poly-Lys

Sequences

Sequence LengthMass (Da)Tools
P56716 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: CA5301316633BD62

FASTA2,095234,388
        10         20         30         40         50         60 
MSDTPSTSFS MIHLTSEGQV PSPRHSNITH PVVAKRISFY KSGDPQFGGV RVVVNPRSFK 

        70         80         90        100        110        120 
TFDALLDSLS RKVPLPFGVR NISTPRGRHS ITRLEELEDG KSYVCSHNKK VLPVDLDKAR 

       130        140        150        160        170        180 
RRPRPWLSSR SISTHVQLCP ATANMSTMAP GMLRAPRRLV VFRNGDPKNK HVVLLSRRIT 

       190        200        210        220        230        240 
QSFEAFLQYL TQVMQCPVAK LYATDGRKVP SLQAVILSSG AVVAAGREPF KPGNYDIQKY 

       250        260        270        280        290        300 
LLPAKLPGIS HRVHQKGKAK IEKRKMSTHM PSDLRPQTDS LISEKTYDCF SDFSVAPENY 

       310        320        330        340        350        360 
LALETHESQS LSTYPSEDDV EKSIVFNQDG TMTVVMKVRF KIKEEETVKW TTTVNRAGLS 

       370        380        390        400        410        420 
NNDEKNKKSS YPGKTDYGPS SLKLEACSLP EDIVDTTQQG SLTEEENTQM TEQQALSCSS 

       430        440        450        460        470        480 
ASWENASMET DIQESQKQVK HFYRPPTPGP RRMRQKKSVI GTVTVVSETE VQEKQFSYSE 

       490        500        510        520        530        540 
ERKGGEKSEY HMFTHSCSKM SSVSNKLVQI GSDNEMESAL ERTRESGSLK SQAINAGAIE 

       550        560        570        580        590        600 
ITSQKVLKMC HNNALPSTAP ENSVVEEGTD NSAVSGTATI KHFRTCGNAN DSFSSITADS 

       610        620        630        640        650        660 
TPTSVNNYSN DRNISELPSV GSPVLTMRLV NEFAHCGLTE KPENRKKVLS SSASKKKKKK 

       670        680        690        700        710        720 
SQQRMITSND KKKVIETKGP PNIAGKIPRA GTTAQERLLQ ESDCPDKGGR VCEQGLNISP 

       730        740        750        760        770        780 
MAIESNNFFP KSNPTFSKNF YKNKLNTFQN PKTQKLLAKR KSRPRKIVST ERLRKQEIGQ 

       790        800        810        820        830        840 
EDKILLHSDS KLCESHLEKQ SLFHVFNILE EDQKVLHRPP FQVEKVARNL KGMAKKSLVP 

       850        860        870        880        890        900 
KVNDLHIMLR NQKKQMGVKL KSGAEVSEQH VTTRADPLAS LKKPDFPEGI PHHSGKSYVK 

       910        920        930        940        950        960 
RWLQNINSYP DFEHRKSGPL CQNRSDVVNY NRNGFLGNNL HTTSSKGNGF LMESNKSKTK 

       970        980        990       1000       1010       1020 
NDNWSGNTNQ ETGKSLVAKD NGEELNKHHC ESQNGSLYDS YLVSLHDNCT LSQTTINEPS 

      1030       1040       1050       1060       1070       1080 
TKSHLSIEKS RPEVKLVYQE MNFATKRQSI EVAIQVDTMG ENVLKDYLPA LLLRHLEAFV 

      1090       1100       1110       1120       1130       1140 
PNNQKHQNGI SQIPGSLAEV VFPSVIDNSS TNLLLAWLLV LNLKRTMNSF CQSDAHKMTN 

      1150       1160       1170       1180       1190       1200 
RPSETAALLE VLKHVAITEE ADDLKAAVAN LMESTKTCSG SSGREQDMLP VNCTASSLHS 

      1210       1220       1230       1240       1250       1260 
VDECNENGSA QKTLLDEGYS VMGDCTSEMV SKSCNSSCEM HMVSKTNPPK QVDDQSDGLL 

      1270       1280       1290       1300       1310       1320 
TSNSCTVSQR STGACFLTDG VYSHEACAQK EGVYEGACLS DETHIPIRDC HTIHSVHSKE 

      1330       1340       1350       1360       1370       1380 
NKCTDDLEST EELKTVDKVP KGLSILADSM YKNDSNVSTF QNVNKLSSQR TLLSKTYLDS 

      1390       1400       1410       1420       1430       1440 
DKDYSPLEEF QNCPRKKIVN KKKSISSDKE ESRTSEEPRS ITNSMTSSER NAISELESFE 

      1450       1460       1470       1480       1490       1500 
ELESQDTSIF NMNVRAEKKS TKETMQKQSE ARMSSELINV SGRKIIEQER RNTAILETTA 

      1510       1520       1530       1540       1550       1560 
RGQVTPPSLA FCYDSNKNTE KEISEGETKM RVKKMVDSME NESYSESSLN FKKHHRSPGT 

      1570       1580       1590       1600       1610       1620 
LDWSDYGSDS ESGYPCKASS NSHNDDSGQE KEPTRGIVKR AIEKLYGKAE IIKPPFFHGS 

      1630       1640       1650       1660       1670       1680 
IHKSQVCPYN SVEVQCAKKT NFYESECQSL VSSEQVSRSS LIFQEFPQVD ANGMGDSFGD 

      1690       1700       1710       1720       1730       1740 
SSIENVTKSS AHDRVFTEKE NGKLIDNGKW LLRENHLWRV SSDNPGMYGN ADTTSVDTLI 

      1750       1760       1770       1780       1790       1800 
DKNSIEVPYS HFGELAPGPT MAELSSSEIE EMTQPLEVKC NYFNFPHGSD SEPFGEDFPD 

      1810       1820       1830       1840       1850       1860 
AQNKTCPKEK IPNHHTEEKG NYPSERLCTS VTQAFVSAGN KVHPVCSDAI KTQPLPGSNI 

      1870       1880       1890       1900       1910       1920 
THGALQEGDS LDKLYALCGQ HCPILTVIIQ PVNEESRGFA YRKDSDIENS LDFQLWMKIY 

      1930       1940       1950       1960       1970       1980 
PFMPQSKKHV FRSDGRNVSV GEEFAGNVIG DLCDQLYFKS MIDLVDQRAN SLGKEINLKK 

      1990       2000       2010       2020       2030       2040 
FQLYLKKSFS DPLSTSLLVV ENRNSVSLSP SSWTDNFKSI DENNNFLNRL PNSSKNPNQV 

      2050       2060       2070       2080       2090 
VRENTNFQFH LELFGQVYLL DICQVEKPLN IKTRSKLEMY YILEGEVLFI WEEEK 

« Hide

References

« Hide 'large scale' references
[1]"Mutations in a gene encoding a new oxygen-regulated photoreceptor protein cause dominant retinitis pigmentosa."
Pierce E.A., Quinn T., Meehan T., McGee T.L., Berson E.L., Dryja T.P.
Nat. Genet. 22:248-254(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION TO 67-76.
Tissue: Retina.
[2]"Progressive photoreceptor degeneration, outer segment dysplasia, and rhodopsin mislocalization in mice with targeted disruption of the retinitis pigmentosa-1 (Rp1) gene."
Gao J., Cheon K., Nusinowitz S., Liu Q., Bei D., Atkins K., Azimi A., Daiger S.P., Farber D.B., Heckenlively J.R., Pierce E.A., Sullivan L.S., Zuo J.
Proc. Natl. Acad. Sci. U.S.A. 99:5698-5703(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 357-367, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[5]"Identification and subcellular localization of the RP1 protein in human and mouse photoreceptors."
Liu Q., Zhou J., Daiger S.P., Farber D.B., Heckenlively J.R., Smith J.E., Sullivan L.S., Zuo J., Milam A.H., Pierce E.A.
Invest. Ophthalmol. Vis. Sci. 43:22-32(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"RP1 is required for the correct stacking of outer segment discs."
Liu Q., Lyubarsky A., Skalet J.H., Pugh E.N. Jr., Pierce E.A.
Invest. Ophthalmol. Vis. Sci. 44:4171-4183(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]"The retinitis pigmentosa 1 protein is a photoreceptor microtubule-associated protein."
Liu Q., Zuo J., Pierce E.A.
J. Neurosci. 24:6427-6436(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
[8]"Distinct gene expression profiles and reduced JNK signaling in retinitis pigmentosa caused by RP1 mutations."
Liu J., Huang Q., Higdon J., Liu W., Xie T., Yamashita T., Cheon K., Cheng C., Zuo J.
Hum. Mol. Genet. 14:2945-2958(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[9]"Essential and synergistic roles of RP1 and RP1L1 in rod photoreceptor axoneme and retinitis pigmentosa."
Yamashita T., Liu J., Gao J., LeNoue S., Wang C., Kaminoh J., Bowne S.J., Sullivan L.S., Daiger S.P., Zhang K., Fitzgerald M.E., Kefalov V.J., Zuo J.
J. Neurosci. 29:9748-9760(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RP1L1, DISRUPTION PHENOTYPE.
[10]"Negative regulation of ciliary length by ciliary male germ cell-associated kinase (Mak) is required for retinal photoreceptor survival."
Omori Y., Chaya T., Katoh K., Kajimura N., Sato S., Muraoka K., Ueno S., Koyasu T., Kondo M., Furukawa T.
Proc. Natl. Acad. Sci. U.S.A. 107:22671-22676(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAK.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF155141 mRNA. Translation: AAD42089.2.
AF291754 Genomic DNA. Translation: AAM17919.1.
BC120927 mRNA. Translation: AAI20928.1.
BC120928 mRNA. Translation: AAI20929.1.
CCDSCCDS14804.1.
RefSeqNP_035413.1. NM_011283.2.
UniGeneMm.294263.

3D structure databases

ProteinModelPortalP56716.
SMRP56716. Positions 34-108.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59493N.
IntActP56716. 1 interaction.
MINTMINT-4132931.
STRING10090.ENSMUSP00000111202.

PTM databases

PhosphoSiteP56716.

Proteomic databases

PaxDbP56716.
PRIDEP56716.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027032; ENSMUSP00000027032; ENSMUSG00000025900.
GeneID19888.
KEGGmmu:19888.
UCSCuc007aex.2. mouse.

Organism-specific databases

CTD6101.
MGIMGI:1341105. Rp1.

Phylogenomic databases

eggNOGNOG313727.
GeneTreeENSGT00530000063898.
HOGENOMHOG000136857.
HOVERGENHBG018173.
OMAEYHMFTH.
OrthoDBEOG7N37DH.
PhylomeDBP56716.
TreeFamTF318770.

Gene expression databases

BgeeP56716.
CleanExMM_RP1H.
GenevestigatorP56716.

Family and domain databases

Gene3D3.10.20.230. 2 hits.
InterProIPR003533. Doublecortin_dom.
[Graphical view]
PfamPF03607. DCX. 2 hits.
[Graphical view]
SMARTSM00537. DCX. 2 hits.
[Graphical view]
PROSITEPS50309. DC. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio297400.
PROP56716.
SOURCESearch...

Entry information

Entry nameRP1_MOUSE
AccessionPrimary (citable) accession number: P56716
Secondary accession number(s): Q548Q8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 6, 2002
Last modified: July 9, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot